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. 2011 Jan 21;77(6):2174–2179. doi: 10.1128/AEM.02690-10

FIG. 3.

FIG. 3.

(A) Production and binding activity of L. paracasei producing surface-anchored ARP1 using a plasmid-based (L. paracasei pAF900-ARP1) and chromosomally integrated (L. paracasei EM233) expression system. (A) Production of ARP1, determined by Western blot analysis of supernatant (s) and cell extract (c). An equivalent of 40 μl supernatant and extract from 3.5 × 107 cells was loaded in each well. For L. paracasei pAF900-ARP1, an arrowhead indicates the band corresponding to intact ARP1 fused to the C-terminal domain of PrtP. (B) Flow cytometry analysis showing the display of ARP1 on the bacterial surface. (C) Flow cytometry analysis showing binding activity of modified L. paracasei for rotavirus. (D) ELISA analysis showing binding activity of modified L. paracasei for rotavirus. Nontransformed L. paracasei and L. paracasei pAF900-S36 were used as negative controls. The coefficient of variation between triplicates is less than 10%.